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. 2013 May 30;6:156. doi: 10.1186/1756-3305-6-156

Figure 1.

Figure 1

Amino acid sequence alignment of tissue inhibitors of metalloproteases (TIMPs) based on predictions of their secondary structures.Homo sapiens TIMP-1 (GenBank accession number XP_010392.1), TIMP-2 (NP_003246.1), TIMP-3 (P35625.2), TIMP-4 (Q99727.1), Canis familiaris TIMP-2 (AF112115.1), Gallus gallus TIMP-2 (AAB69168.1), Oryctolagus cuniculus TIMP-2 (AAB35920.1), Mus musculus TIMP-1 (P12032.2), TIMP-2 (P25785.2), TIMP-3 (P39876.1), TIMP-4 (Q9JHB3.1), Drosophila melanogaster TIMP (AAL39356.1), Caenorhabditis elegans CRI-2 (K07C11.5), Ancylostoma caninum TMP-1 (AF372651.1), TMP-2 (EU523696.1), Ancylostoma duodenale TIMP-1 (ABP88131.1), Necator americanus (NECAME_13168, NECAME_07191, NECAME_01063, NECAME_05356, NECAME_05357, NECAME_14664, NECAME_08457 and NECAME_08458), Dictyocaulus filaria (1495356.2; http://www.gasserlab.org), Oesophagostomum dentatum (E59TEJM01BU99S and E59TEJM02GRTKW; http://www.gasserlab.org), Ascaris suum (GS_21732, GS_04796, GS_08199; http://www.wormbase.org), Schistosoma haematobium A_01727, Schistosoma mansoni Smp_087690 and Schistosoma japonicum Sjp_0053050 (http://www.genedb.org). Ancylostoma ceylanicum AceES-2 (GenBank Q6R7N7) is also included.